ID A0A1S2R8H6_9BACI Unreviewed; 221 AA.
AC A0A1S2R8H6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase {ECO:0000256|HAMAP-Rule:MF_01680};
DE Short=HK-MTPenyl-1-P phosphatase {ECO:0000256|HAMAP-Rule:MF_01680};
DE EC=3.1.3.87 {ECO:0000256|HAMAP-Rule:MF_01680};
GN Name=mtnX {ECO:0000256|HAMAP-Rule:MF_01680};
GN ORFNames=BIV60_10985 {ECO:0000313|EMBL:OIK14839.1};
OS Bacillus sp. MUM 116.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1678002 {ECO:0000313|EMBL:OIK14839.1, ECO:0000313|Proteomes:UP000180019};
RN [1] {ECO:0000313|EMBL:OIK14839.1, ECO:0000313|Proteomes:UP000180019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUM 116 {ECO:0000313|EMBL:OIK14839.1,
RC ECO:0000313|Proteomes:UP000180019};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Bacillus sp. MUM 116.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Dephosphorylates 2-hydroxy-3-keto-5-methylthiopentenyl-1-
CC phosphate (HK-MTPenyl-1-P) yielding 1,2-dihydroxy-3-keto-5-
CC methylthiopentene (DHK-MTPene). {ECO:0000256|HAMAP-Rule:MF_01680}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate + H2O =
CC 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate;
CC Xref=Rhea:RHEA:14481, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:49252, ChEBI:CHEBI:59505; EC=3.1.3.87;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01680};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate:
CC step 4/6. {ECO:0000256|HAMAP-Rule:MF_01680}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. MtnX family.
CC {ECO:0000256|HAMAP-Rule:MF_01680}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OIK14839.1}.
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DR EMBL; MLYR01000038; OIK14839.1; -; Genomic_DNA.
DR RefSeq; WP_071355782.1; NZ_MLYR01000038.1.
DR AlphaFoldDB; A0A1S2R8H6; -.
DR STRING; 1678002.BIV60_10985; -.
DR OrthoDB; 9804940at2; -.
DR UniPathway; UPA00904; UER00877.
DR Proteomes; UP000180019; Unassembled WGS sequence.
DR GO; GO:0043716; F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR CDD; cd07524; HAD_Pase; 1.
DR Gene3D; 3.90.1470.20; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR HAMAP; MF_01680; Salvage_MtnX; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR017718; HAD-SF_hydro_IB_MtnX.
DR InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR01489; DKMTPPase-SF; 1.
DR NCBIfam; TIGR01488; HAD-SF-IB; 1.
DR NCBIfam; TIGR03333; salvage_mtnX; 1.
DR PANTHER; PTHR28181:SF2; PHOSPHORIC MONOESTER HYDROLASE; 1.
DR PANTHER; PTHR28181; UPF0655 PROTEIN YCR015C; 1.
DR Pfam; PF12710; HAD; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01680};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01680};
KW Methionine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01680};
KW Reference proteome {ECO:0000313|Proteomes:UP000180019}.
SQ SEQUENCE 221 AA; 25274 MW; 79BB59642E5D7D7C CRC64;
MRKPIIYCDF DGTITESDNI IAIMKKFAPP GWETIKDQIL SQQISISEGV GKLFSLLPSD
WKDEITAFAI ENAKIRPGFK EFVEFTRNEK IPFYIISGGI DFFLYPILEE FGLFDGVYCN
ESDFSGETIK ILWPHECDEF CSNHCGCCKP SVIRQLEKGQ DHFKIVIGDS VTDLEAAKQA
NFVLARDLLQ EKCVEWGINH KGFITFYDCI EEIKKELGWV S
//
